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JPS62283199A - Oxygen detergent composition - Google Patents

Oxygen detergent composition

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Publication number
JPS62283199A
JPS62283199AJP61131674AJP13167486AJPS62283199AJP S62283199 AJPS62283199 AJP S62283199AJP 61131674 AJP61131674 AJP 61131674AJP 13167486 AJP13167486 AJP 13167486AJP S62283199 AJPS62283199 AJP S62283199A
Authority
JP
Japan
Prior art keywords
lipase
composition according
detergent
composition
builder
Prior art date
Legal status (The legal status is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the status listed.)
Granted
Application number
JP61131674A
Other languages
Japanese (ja)
Other versions
JPH0134560B2 (en
Inventor
ダヴイド・トーム
トン・スウアルトーフ
ヤン・マート
Current Assignee (The listed assignees may be inaccurate. Google has not performed a legal analysis and makes no representation or warranty as to the accuracy of the list.)
Unilever NV
Original Assignee
Unilever NV
Priority date (The priority date is an assumption and is not a legal conclusion. Google has not performed a legal analysis and makes no representation as to the accuracy of the date listed.)
Filing date
Publication date
Application filed by Unilever NVfiledCriticalUnilever NV
Publication of JPS62283199ApublicationCriticalpatent/JPS62283199A/en
Publication of JPH0134560B2publicationCriticalpatent/JPH0134560B2/ja
Grantedlegal-statusCriticalCurrent

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Abstract

Translated fromJapanese

(57)【要約】本公報は電子出願前の出願データであるた
め要約のデータは記録されません。
(57) [Summary] This bulletin contains application data before electronic filing, so abstract data is not recorded.

Description

Translated fromJapanese

【発明の詳細な説明】本発明は酵素洗剤組成物に関する。特に本発明は、脂肪
分解酵素を含有する酵素洗剤組成物に関する。
DETAILED DESCRIPTION OF THE INVENTION The present invention relates to enzyme detergent compositions. In particular, the present invention relates to enzymatic detergent compositions containing lipolytic enzymes.

酵素洗剤組成物は当業界で公知である。洗剤組成物の配
合用に多種類のPr素が促案されているが、主としてプ
ロテアーゼ及びアミラーゼが注目されている。リパーゼ
も洗剤組成物用酵素として考えられているが、一般的洗
剤組成物用リパーゼに直接像る従来技術は比較的少ない
Enzyme detergent compositions are known in the art. Although many types of Pr elements have been proposed for formulation in detergent compositions, proteases and amylases have received most attention. Although lipase is also considered as an enzyme for detergent compositions, there is relatively little prior art that directly addresses lipases for general detergent compositions.

B P  1,372.034には、p seudom
onas  5tlJtZQriΔT CC19,15
4のようなp SeUdOmOnaSグループの微生物
より産生されたリパーゼを、特定のノニオン洗剤活性物
質と任意に特定のアニオン洗剤活性化合物を含む衣類浸
漬用(soaking fabrics)洗剤組成物中
に使用する旨が開示されている。しかしながら、“任意
のかつ何れの洗剤組成物に脂肪分解酵素を添加しても、
(記載した姐く)酵素活性及び洗浄効率の点で満足かつ
許容され得る洗剤組成物が得られる訳ではないパことが
明らかであった。洗剤組成物の各種成分が脂肪分解酵素
に対してマイナスの影響を示すことが知見された。
B P 1,372.034 contains p-seudom.
onas 5tlJtZQriΔT CC19,15
Discloses the use of lipases produced by microorganisms of the pSeUdOmOnaS group such as 4 in soaping fabric detergent compositions comprising certain nonionic detergent actives and optionally certain anionic detergent active compounds. has been done. However, “the addition of lipolytic enzymes to any and all detergent compositions does not
It was clear that a detergent composition that was satisfactory and acceptable in terms of enzyme activity and cleaning efficiency (as described above) was not obtained. It has been found that various components of detergent compositions exhibit negative effects on lipolytic enzymes.

B P  1,442,418及び1,442,419
には二段階洗1g方法が記載されている。該方法は、リ
パーゼ含有液に浸漬させる工程とその後の洗ふ(含有洗
浄液で洗濯する工程とから成る。
B P 1,442,418 and 1,442,419
describes a two-stage washing 1g method. The method consists of a step of immersing in a lipase-containing liquid and a subsequent washing step (washing with a washing liquid containing lipase).

13 p  1,442.41’lに記載の発明におい
ては、゛リパーゼ含有液゛′はクレームされた1種もし
くはそれ以上のリパーゼと水溶性ホウ酸ナトリウム塩(
borax 5alt)とから構成されている。所要に
より慣用の洗浄性界面活性剤またはビルダーを含有させ
ても良い旨が記載されているが、界面活性剤またはビル
ダーの存在下での有効性は立証されていない。B P 
1,442,418の“リパーゼ含有液”は、クレーム
された1種もしくはそれ以上のリパーゼとホウ酸ナトリ
ウムとc a2 +もしくはM Cl ”−(オンとか
ら構成されている。界面活性剤も記載されているが、界
面活性剤溶液における有効性を示す証拠は促示されてい
ない。c a2 +及び/又はMg2+イオンと結合す
るビルダーはこれらの予洗液から明白に排除されている
。何れにしても、上記した両発明に記載の洗濯方法では
別個に調製された2種の材料が必要であり、実用性に乏
しい。
13 p. 1,442.41'l, the lipase-containing liquid 'is composed of one or more claimed lipases and a water-soluble sodium borate salt (
borax 5alt). Although it is stated that a conventional detersive surfactant or builder may be included if necessary, effectiveness in the presence of a surfactant or builder has not been proven. B P
The "liquid containing lipase" of No. 1,442,418 is composed of one or more of the claimed lipases, sodium borate, and ca2 + or M Cl "-(one). A surfactant is also described. However, no evidence of effectiveness in surfactant solutions has been suggested. Builders that bind Ca2+ and/or Mg2+ ions are clearly excluded from these prewash solutions. However, the washing methods described in both of the above-mentioned inventions require two separately prepared materials, and are therefore impractical.

J ournal  of  A pplied  B
 iochemistry  2(1980) 、  
D、218〜229のA ndrceらの文献には、洗
剤成分としてのリパーゼに関する研究報告が記載されて
いる。、試験した2種の市販のリパーゼ(膵リパーゼと
りゾーブスリパーピ)は典型的な洗浄性アニオン及びノ
ニオン界面活性剤の混合物を含む活性系の溶液中で不安
定であるとの結論が記載されている。リパーゼはアニオ
ン洗剤の存在下で不活性化され、その程度は膵リパーゼ
がRhizopusリパーゼよりやや小さいと推定され
ると記載されている。And reeらは更に、試験し
たリパーゼによりノニオン洗剤調に物の洗浄作用が改善
されるが、前記改善は洗剤調製物中のノニオる。
Journal of A applied B
iochemistry 2 (1980),
D, 218-229, Andrce et al. describes a research report on lipase as a detergent component. describe the conclusion that the two commercially available lipases tested (pancreatic lipase and zobus lipase) are unstable in solutions of active systems containing mixtures of typical detersive anionic and nonionic surfactants. It is stated that lipase is inactivated in the presence of anionic detergents, and the degree of inactivation is estimated to be slightly lower for pancreatic lipase than for Rhizopus lipase. Furthermore, the lipases tested improved the cleaning action of non-ionic detergents, but said improvement was due to non-ionic detergents in detergent formulations.

最近公開されたE P 0.130.064には、洗剤
添加剤としてm旦ユ」 旦■■」三由来のリパーゼを使
用する旨が記載されている。この明細書に例示されてい
る洗剤組成物はノニオン洗剤とアニオン洗剤の8合物、
或いはノニオン洗剤のみから成る。
The recently published EP 0.130.064 describes the use of lipases derived from ``mdanyu'' and ``dan■■'' as detergent additives. The detergent compositions exemplified in this specification include eight combinations of nonionic detergents and anionic detergents;
Or it consists only of nonionic detergent.

上記したように、何れの従来技術も、洗剤組成勘に特定
のりパーぎを使用すること或いはリパーゼを配合させる
ために特定の洗剤組成物及び/又は洗濯系(wash 
r(!(]1llleS)を調%l−することを教示し
ているに過ぎない。
As mentioned above, none of the prior art requires the use of a specific glue or the formulation of a specific detergent composition and/or wash system in order to incorporate lipase into the detergent composition.
It merely teaches how to modulate r(!(]1lleS).

本発明の目的は、リパーゼを配合させることにより全体
的な洗浄性能が改善されるとともに洗浄力が大きく改善
されるリパーゼ含有洗剤組成物を促供することにある。
An object of the present invention is to provide a lipase-containing detergent composition in which the overall cleaning performance is improved and the detergency is significantly improved by incorporating lipase.

本発明者らは、洗剤活性物質としてアニオン合成洗剤と
ビルグーとして水溶性h−n及び/又は、黒磯ビルグー
塩を含むビルト洗剤組成物中に成る種のリパーゼを配合
(1nclusion)させると洗浄力が全体的に向上
することを知見した。
The present inventors have discovered that the detergent power can be improved by incorporating a type of lipase consisting of an anionic synthetic detergent as a detergent active substance and a water-soluble hn and/or Kuroiso virgoux salt as a detergent active substance into a built-in detergent composition. We found that there was an overall improvement.

従来皮術とは対照的に、本発明により促供されるリパー
ゼ含有洗浄組成物ではより低温でも通常通りに洗濯を実
施することができる。従って、洗ひ組成物を特別に注意
深く選択したり、特定の洗濯或いは浸漬工程を行わずに
、またはリパーゼ含有組成物で衣類を長期間に処理しな
くとも、リパーゼの利点が得られる。
In contrast to conventional skin techniques, the lipase-containing cleaning composition facilitated by the present invention allows laundering to be carried out normally even at lower temperatures. Thus, the benefits of lipases are obtained without particularly careful selection of wash compositions, specific washing or soaking steps, or long-term treatment of garments with lipase-containing compositions.

本発明で使用され得るリパーゼには、pseudolionas  fluorescens
   l△M  +057より産生されたリパーゼであ
って、リパーゼの抗体と正の免疫学交差反応(pos口
ive immunologicalCross−re
action)を示すリパーゼが包含される。
Lipases that can be used in the present invention include pseudolionas fluorescens
The lipase produced by LΔM+057 has positive immunological cross-reactivity with antibodies of lipase.
lipases that exhibit action) are included.

このリパーゼ及びその精製方法については、1978年
2J]24日付で公開された待間昭53−20487号
公報に記載されている。このリパーゼ(よ、商品名リバ
ーd p ” A nano”として天野¥J薬■より
市販されている(以下、これを“′Δmano −P 
”と略記する)。本発明のりパーピは、オクテルロニ−
(ACta、  Mad、 3can、、  133.
 I)、76−79(1950))による標準的な公知
の免疫拡散法に従って、A mano −p抗体と正の
免疫学的交差反応を示すものでなければなら/iい。
This lipase and its purification method are described in Machima Sho 53-20487, published on 2J]24, 1978. This lipase (Yo) is commercially available from Amano\J Yakuhin under the trade name River dp ``A nano'' (hereinafter referred to as ``'Δmano-P'').
(abbreviated as “Oxterrony”).
(ACta, Mad, 3can,, 133.
The antibody must exhibit positive immunological cross-reactivity with the A mano-p antibody according to standard known immunodiffusion methods (I), 76-79 (1950)).

抗血清は次のようにして作成される。Antiserum is prepared as follows.

等8量の0.1量g/d抗原と(完全もしくは不完全)
フロインドアジュバントをエマルジョンが得られるまで
混合するつ下記の順序でエマルジョンリンプル2−を2
羽の雌家兎に注入した。
equal 8 doses of 0.1 g/d antigen (complete or incomplete)
Mix Freund's adjuvant until an emulsion is obtained.
injected into female rabbits.

0白目;完全70インドアジュバント中抗原4日目;完
全フロインドアジュバント中抗原32日目:不完全フロ
インドアジュバント中抗原60日目:不完全フロインド
アジュバント中抗原グースター所要の抗体を含む血清を、67日0に採血した1疑固而
液を遠心して得た。
0 whites of the eyes; 4th day of antigen in complete Freund's adjuvant; 32nd day of antigen in complete Freund's adjuvant: 60th day of antigen in incomplete Freund's adjuvant: Antigen in incomplete Freund's adjuvant. A sample of blood sample 1 was obtained by centrifugation.

抗−A+mano−P−リパーゼ抗血清の力価は、オフ
テルロニー法に従って抗原及び抗+fi+清を系列希釈
しながら沈降反応を観察することにより決定される。抗
血清の25希釈度は、01■/dの抗原濃度で目に見え
る沈降物を生ずる希釈度ぐある。
The titer of the anti-A+mano-P-lipase antiserum is determined by observing the precipitation reaction while serially diluting the antigen and anti+fi+ supernatant according to the Ophterlony method. A 25 dilution of antiserum is the dilution that produces a visible precipitate at an antigen concentration of 0.1 /d.

上記した如< A mano −P FFi体と正の免
疫学的交差反応を示すリパーゼが全て、本発明のリパー
ゼである。リパーゼの!II!梨的な例が、Amanθ
−Pリパーゼ、 P scudomonas  セ且引
−F E RM  P1339  由来のリバ〜ゼ(商
品名 Δmano −B ) 。
All lipases that exhibit positive immunological cross-reactivity with the above-mentioned A mano-P FFi bodies are lipases of the present invention. Of lipase! II! A typical example is Amanθ
-P lipase, P lipase (trade name Δmano-B) derived from P scudomonas FE RM P1339.

SOlldomOnaS  n1troreducOn
s  Var。
SOlldomOnaS n1troreducOn
s Var.

1i旧としυj匹J」エ FERM  P  1338
由来のリパーゼ(商品名 △manO−CE S ) 
、  hroIIlobacter−■銭ム」(1?I
えば hromobacter  viscosum 
var。
1i old and υj animals J'd FERM P 1338
derived lipase (product name △manO-CES)
, hroIIlobacter-■zenmu'' (1?I
For example, hromobacter viscosum
var.

li閃とハリ:i(um  N RRL B 3673
)由来のリパーゼ(東洋M m tmより市販) 、 
Chromobactcrviscosun+  リパ
ーゼ(米国のUS  B iochemicalCor
p及びオランダの□ 1osynth にO−より市販
)。
li flash and firmness: i(um N RRL B 3673
) derived lipase (commercially available from Toyo Mmtm),
Chromobactcrviscosun + lipase (US Biochemical Cor.
(commercially available from O- to □1osynth, Netherlands).

並びに圧胆U匹健」 史1ad邸l」由来のりパービで
ある。
In addition, it is a parby derived from "History 1 ad residence l".

本発明の好ましいリパーゼは、東洋8II造((2)よ
り市販されティるC hro+nobactQr  v
iscosum  Var。
A preferred lipase of the present invention is Chro+nobactQrv, commercially available from Toyo 8II Co., Ltd. ((2)).
iscosum Var.

1i旧しいり」匹till  IIIRLB 3673
由来のリパーゼ或いはpseudomonas  gl
adioli由来のリパーゼの抗体と正の免疫学的交差
反応を示すものである。
1i old Shiiri” till IIIRLB 3673
lipase or pseudomonas gl
This shows a positive immunological cross-reactivity with the antibody of lipase derived from C. adioli.

上記した好ましいリパーゼとしては、A man。The preferred lipase mentioned above is Aman.

−p、 All1ano−F3. Amano−CES
、東洋醸造四より市販されているΩ」■四」旦立倶:t
er  viscosum(例えば hromobac
ter  viscosum  var。
-p, All1ano-F3. Amano-CES
, commercially available from Toyo Jozo 4.
er viscosum (e.g. hromobac
ter viscosum var.

1io1ticum  NRRLB  3673)由来
(7)’Jハーゼ、米国のU S  B iochem
ical  Corp、及びオランダのD 1osyn
th  COより市販されているChromobact
er  viscosumリパーゼ並びにP seud
omonas  gladioli由来のリバーげが例
示される。
1io1ticum NRRLB 3673) (7)' J Hase, US Biochem, USA
ical Corp, and D 1osyn of the Netherlands.
Chromobact commercially available from th CO
er viscosum lipase and P seud
An example is reverb derived from Omonas gladioli.

本発明のリパーゼは洗剤組成物中に配合され、その配合
(6)は畿終洗剤組成物の脂肪分解II?素活性が 1
00〜Q、O05LU/PI、好ましく ハ25〜0.
051U/ηであるような伯である。
The lipase of the present invention is blended into a detergent composition, and its formulation (6) is the lipolysis II? of the Kishu detergent composition. elementary activity is 1
00~Q, O05LU/PI, preferably Ha25~0.
051U/η.

リパーゼ単位(LU)ハ、30℃、  I)H=9.0
I7)条件下で1分間あたりに1μmolの滴定可能な
脂肪酸を生ずるリパーゼの量である。なお、基質ハ5I
llIIO1ノドリス緩衝剤中ニ13mmol −Ca
 2+及び20m1ol −N a Ciの存在下でオ
リーブ油3.3wt%及びアラビアゴム3.3wt%を
含むエマルジョンである。
Lipase unit (LU) C, 30°C, I) H = 9.0
I7) is the amount of lipase that yields 1 μmol of titratable fatty acids per minute under conditions. In addition, the substrate C5I
13 mmol -Ca in llIIO1 Nodris buffer
An emulsion containing 3.3 wt% olive oil and 3.3 wt% gum arabic in the presence of 2+ and 20 m1ol -N a Ci.

勿論、上記リパーゼの混合物も使用可能である。Of course, mixtures of the above lipases can also be used.

リパーゼは未精製物のままでも、また例えばフェニルセ
ファロース充填カラム法の如き公知の吸着法により精製
した[1物も使用されうる。
Lipase can be used either unpurified or purified by known adsorption methods, such as the phenyl Sepharose packed column method.

本発明のリパーゼを配合する洗剤組成物は、洗剤活性物
質として少なくとも1piのアニオン合成洗剤活性物質
のみを含む。この種の洗剤活性化合物も当業者には公知
であり、その適切な例が3chwartz 、 per
ry及びB erch著” 3 urface−A c
tive A gents and [) etrgc
nts” 、 vol、 I(1949)及びvol、
 II (+958)に詳しく記載されている。
Detergent compositions incorporating the lipases of the invention contain only at least 1 pi of anionic synthetic detergent actives as detergent actives. Detergent active compounds of this type are also known to those skilled in the art, suitable examples of which are described in 3chwartz, per.
ry and Berch” 3 surface-A c
tive A gents and [)etrgc
nts”, vol. I (1949) and vol.
II (+958).

洗剤組成物中に占めるアニオン洗剤活性物質の量は1へ
・40重徹%であり、通常2〜35重量%、好ましくは
5〜30重量%である。
The amount of anionic detergent active in the detergent composition is 1 to 40% by weight, usually 2 to 35% by weight, preferably 5 to 30% by weight.

洗剤組成物が更に、1〜55重量%、好ましくは5〜3
0川吊%の1種もしくはそれ以上の水溶性の有機及び/
又は無殿ビルグー塩を含み得る。典型的な前記ごルダー
塩として、オルト−、ピローおよび(トリ)ポリリン酸
のアルカリ金属1冨、アルカリ金属炭酸塩、アルカリ金
属クエンfl Jg、アルカリ金属ニトリロトリ酢酸塩
等及び各種水溶性ビルグー塩の混合物が例示される。好
ましくはトリポリリン酸ペンタナトリウム及び/又は炭
酸すトリウムが使用される。更に組成物が1〜35重量
%の漂白剤または漂白剤とその活性剤から成る漂白系を
含んでいてもよい。この点に関して、本発明のリパーゼ
は、本発明以外の他のリパーゼに比べ炉て組成物中に存在する漂白剤もしく漂白系により受ける
影響がかなり少ないという驚くべき知見も得られた。
The detergent composition further comprises 1 to 55% by weight, preferably 5 to 3% by weight.
0% of one or more water-soluble organic and/or
Or it may contain free virgoos salt. Typical of the above salts include alkali metal 1-rich ortho-, pyro- and (tri)polyphosphoric acids, alkali metal carbonates, alkali metal citric acids, alkali metal nitrilotriacetates, etc., and mixtures of various water-soluble virgoux salts. is exemplified. Preferably pentasodium tripolyphosphate and/or sodium carbonate are used. Additionally, the composition may contain from 1 to 35% by weight of a bleaching agent or a bleaching system consisting of a bleaching agent and its activator. In this regard, the surprising finding has also been made that the lipases of the present invention are much less affected by bleaching agents or bleaching systems present in the composition than other lipases other than the present invention.

組成物が、発泡剤、消泡剤、腐食防止剤、汚れ浮遊11
111 (Rail−suspending agen
ts) 、金属イオン封鎖剤、汚れ再付着防止剤、香料
1着色剤、Vi−累安定化剤、′fA白剤等を含んでい
てもよい。また組成物がリパーゼ以外の酵素、例えばプ
ロテアーゼ。
The composition is a foaming agent, an antifoaming agent, a corrosion inhibitor, and a dirt floating agent.
111 (Rail-suspending agent
ts), a sequestrant for metal ions, a stain redeposition preventive agent, a fragrance 1 coloring agent, a Vi-stable stabilizer, a 'fA whitening agent, and the like. The composition may also contain enzymes other than lipases, such as proteases.

アミラーゼ、オキシダーぜ及びセルラーゼを含んでいて
もよい。この点に関して、本発明のリパーゼの場合クリ
ーンなモデルシステムにおいてプロテアーゼの存在下で
はその活性が急速に消失するが、洗iRR内の実際の洗
濯条件下ではプロテアーゼの存在下でもリパーゼによる
実質的な作用が得られ′るという驚くべき知見が得られ
た。
May contain amylase, oxidase and cellulase. In this regard, in the case of the lipase of the present invention, its activity rapidly disappears in the presence of protease in a clean model system, but under actual washing conditions in the washed iRR there is no substantial effect by the lipase even in the presence of protease. The surprising finding was that it was possible to obtain

本発明の組成物は任意の所望の形態、例えば粉末、棒、
ペースト、液体等の形態で調製され得る。
The compositions of the invention may be in any desired form, e.g. powder, bar,
It can be prepared in the form of paste, liquid, etc.

前記したように、本発明の組成物は全体的に優れた洗υ
作用、特により低温でその作用を示す。
As mentioned above, the composition of the present invention provides excellent overall cleaning properties.
action, especially at lower temperatures.

従来リパーゼは特殊な条件下でVj定の効果しか示さ〆
ないと考えられていたのに対して、本発明のリパーゼを
配合した洗剤組成物ではnC1記したように全体的に優
れた洗浄性能を示すことは驚くべきことである。
It was previously thought that lipase only showed a certain effect under special conditions, but the detergent composition containing the lipase of the present invention has excellent overall cleaning performance as noted in nC1. It's amazing to show.

以下、本発明を実施例に基いて更に説明する。The present invention will be further explained below based on Examples.

実施例1次の洗剤組成物に任意に本発明のリパーゼを含有させ、
洗濯テストを実施した。使用したリパーゼはΔmano
−Pであり、その濃度は15LIJ/Idであった。
Example 1 The following detergent composition optionally contains a lipase of the present invention,
A washing test was conducted. The lipase used was Δmano
-P, and its concentration was 15LIJ/Id.

次の条件下で洗濯テストを行った。A washing test was conducted under the following conditions.

無!!IM料、タンパク、パーム油を含有する混合物で
汚したコツトンクロスを35LJ/lの洗剤組成物を含
有する20℃の洗濯液に混油させ、 15分間手洗い侵
、1回あたり2分を要して3回リンスした。洗濯侵のク
ロスを再び汚し、洗濯した。汚す(soi l ing
)/洗濯工程を4回繰り返した。水硬度は8°GHであ
った。
Nothing! ! Cotton cloth soiled with a mixture containing IM agent, protein, and palm oil was mixed with a 20°C washing liquid containing 35 LJ/l of detergent composition, and washed by hand for 15 minutes, requiring 2 minutes per wash. and rinsed three times. The washed cloth was soiled again and washed. soiling
)/The washing process was repeated four times. Water hardness was 8°GH.

浸漬、洗濯及びリンス中の液体/クロス比(よ夫々9.
3.20であった。4回目の洗濯(D、クロスの反射率
及びクロス上に残留ツる脂肪質物質のパーセンテージを
測定した。反射率は、光路にUvフィルターを設置し反
射計を用いて460niで測定した。乾燥させたクロス
を石油エーテルで抽出し、溶媒を留出させた後残存する
脂肪質1tIJ質< rattymatter)の量(
%FM)を測定した。
Liquid/cloth ratio during soaking, washing and rinsing (9.
It was 3.20. 4th wash (D) The reflectance of the cloth and the percentage of fatty substances remaining on the cloth were measured. The reflectance was measured at 460 ni using a reflectometer with a UV filter in the light path. After extracting the cloth with petroleum ether and distilling off the solvent, the amount (
%FM) was measured.

次の結果が1!1られた。The next result was 1!1.

実施例2次の条件下でターボトメ−ター(Tcrgo℃〇−mO
℃cr)を用い、マルチサイクル汚れ洗濯システム(m
ulticycle 5oiled wash sys
tem)における各神洗剤組成物の刊北を比較した。
Example 2 A turbotometer (Tcrgo℃〇-mO
℃cr) and a multi-cycle dirt washing system (m
ultimate cycle 5 oiled wash sys
The publication of each detergent composition in TEM) was compared.

撹           痒 ;     50rpm
洗濯温度及び時間:  至潟′c10分間す     
 ン     ス :     3 × 2 分水  
   硬     度 :    17° GHプロテ
ア−ぜ濃度:   20GU/dリパ一ゼ濃度二  1
LU#!テ ス ト 布;  コツトンクロス汚      れ:  バーム浦ト粉ミルク次の洗剤組
成物を使用した。
Stirring itching; 50rpm
Washing temperature and time: 10 minutes
Source: 3 x 2 water divisions
Hardness: 17° GH protease concentration: 20GU/d Lipase concentration 2 1
LU#! Test cloth; Cotton cloth soiled: Balm urato powdered milk The following detergent composition was used.

A、30%  ドデシルペンピンスルボン酸ナトリウム30%  硫M少トリウム30%  トリポリリン酸ナトリウム10%  ケイ酸ナトリウムB、八と同じ。但しトリポリリン酸ナトリウムに代えて
ゼオライトを使用した。
A, 30% Sodium dodecylpenpine sulfonate 30% Minor thorium sulfate 30% Sodium tripolyphosphate 10% Sodium silicate B, Same as 8. However, zeolite was used instead of sodium tripolyphosphate.

組成物の使用温度は27/lであった。The working temperature of the composition was 27/l.

4回目の洗濯後に得られた結果は次の通りである。The results obtained after the fourth wash are as follows.

実施例3次の組成物について、ターボトメ−ター(4マルチサイ
クル汚れ洗濯)を用い硬度8°GHの水において20℃
で14分間デストした。濃度は1.3g/lであった。
Example 3 The following compositions were tested at 20°C in water with a hardness of 8°GH using a turbotometer (4 multi-cycle soil washing).
It was dead for 14 minutes. The concentration was 1.3 g/l.

東洋醸造リパーゼを3LU/ai!の濃度で使用した。3LU/ai of Toyo Brewery Lipase! It was used at a concentration of

コツトン、ポリエステル/コツトン及びポリエステルク
ロスをテストした。
Cotton, polyester/cotton and polyester cloth were tested.

テストした組成物は次の組成を有する。The composition tested had the following composition:

15% 直鎖C12アルキルベンゼンスルホン酸塩20
% ケイ酸ナトリウム35% 炭酸ナトリウム25% lj!I酸ナトリウム5% 少量成分十水分4回目の洗濯侵得られた結果は次の通りである。
15% linear C12 alkylbenzene sulfonate 20
% Sodium silicate 35% Sodium carbonate 25% lj! Sodium I acid 5% Small component sufficient moisture The results obtained after the 4th wash are as follows.

なお、−シーリパーゼ非含有;+シーリパーゼ含有を表
わす。
In addition, - sea lipase not contained; + sea lipase contained is represented.

衷11111LtJ/Idリパ一ゼ温度の各種リパーゼを有する実
施例1の組成物について、ターボトメ−ターを用い硬度
17°GHの水で洗)1実験を行った。組成物調度は2
g/lであり、パーム油及び粉ミルクの温合物で汚した
コツトンクロスを用いてテストを行ったa44回目洗濯
後反射率及び%FMを測定した。
An experiment was conducted on the composition of Example 1 containing various lipases having a lipase temperature of 1111 1 LtJ/Id (washed with water having a hardness of 17°GH) using a turbotometer. Composition preparation is 2
g/l and tested using cotton cloth stained with a warm mixture of palm oil and powdered milk.The reflectance and %FM were measured after the 44th wash.

次のような結果が得られた。The following results were obtained.

Claims (9)

Translated fromJapanese
【特許請求の範囲】[Claims](1)洗剤活性化合物としてのアニオン合成洗剤とビル
ダーとリパーゼとから成る洗剤組成物であって、前記ビ
ルダーが水溶性の無機もしくは有機ビルダー塩であり、
前記リパーゼが微生物¥Pseudomonasflu
orescens¥ IAM1057より産生され得か
つリパーゼ抗体と正の免疫学的交差反応を示すリパーゼ
であることを特徴とする組成物。
(1) A detergent composition comprising an anionic synthetic detergent as a detergent active compound, a builder, and a lipase, the builder being a water-soluble inorganic or organic builder salt,
The lipase is a microorganism¥Pseudomonasflu
A composition characterized in that it is a lipase that can be produced from S. orescens IAM1057 and exhibits positive immunological cross-reactivity with lipase antibodies.
(2)ビルダーがトリポリリン酸ペンタナトリウムであ
る特許請求の範囲第1項に記載の組成物。
(2) The composition according to claim 1, wherein the builder is pentansodium tripolyphosphate.
(3)ビルダーが炭酸ナトリウムである特許請求の範囲
第1項に記載の組成物。
(3) The composition according to claim 1, wherein the builder is sodium carbonate.
(4)ビルダーがトリポリリン酸ペンタナトリウムと炭
酸ナトリウムの混合物である特許請求の範囲第1項に記
載の組成物。
(4) The composition according to claim 1, wherein the builder is a mixture of pentansodium tripolyphosphate and sodium carbonate.
(5)リパーゼが、¥Chromobacter¥ ¥
viscosum¥var.¥lipolyticum
¥ NRRLB3673または¥Pseudomona
s¥ ¥gladioli¥より産生され得かつリパー
ゼ抗体と正の免疫学的交差反応を示す特許請求の範囲第
1項に記載の組成物。
(5) Lipase is ¥Chromobacter¥ ¥
viscosum¥var. ¥lipolyticum
¥NRRLB3673 or ¥Pseudomona
2. The composition according to claim 1, which can be produced from S. gladioli. and exhibits positive immunological cross-reactivity with lipase antibodies.
(6)正の免疫学的交差反応を示すリパーゼが¥Pse
udomonas¥及び¥Chromobacter¥
属の株より産生され得るリパーゼである特許請求の範囲
第1項に記載の組成物。
(6) Lipase showing positive immunological cross-reactivity is ¥Pse
udomonas¥and¥Chromobacter¥
The composition according to claim 1, which is a lipase that can be produced by a strain of the genus.
(7)リパーゼが¥Pseudomonas¥ ¥fl
uorescens¥、Pseudmonas¥ ¥f
ragi¥、¥Pseudomonas¥¥nitro
reductans¥ var.¥lipolytic
um¥、¥Pseudomonas¥ ¥gladio
li¥及びChromobacter¥¥viscos
um¥の株より産生され得る特許請求の範囲第1項に記
載の組成物。
(7) Lipase is ¥Pseudomonas¥fl
uorescens¥、Pseudmonas¥¥f
ragi¥、¥Pseudomonas¥¥nitro
reductans¥ var. ¥lipolytic
um¥、¥Pseudomonas¥¥gladio
li¥ and Chromobacter¥¥viscos
The composition according to claim 1, which can be produced from a strain of um\.
(8)更に漂白剤を含む特許請求の範囲第1項に記載の
組成物。
(8) The composition according to claim 1, further comprising a bleaching agent.
(9)更にタンパク分解酵素を含む特許請求の範囲第1
項に記載の組成物。
(9) Claim 1 further includes a proteolytic enzyme.
The composition described in Section.
JP61131674A1985-06-111986-06-06Oxygen detergent compositionGrantedJPS62283199A (en)

Applications Claiming Priority (2)

Application NumberPriority DateFiling DateTitle
GB85147081985-06-11
GB858514708AGB8514708D0 (en)1985-06-111985-06-11Enzymatic detergent composition

Publications (2)

Publication NumberPublication Date
JPS62283199Atrue JPS62283199A (en)1987-12-09
JPH0134560B2 JPH0134560B2 (en)1989-07-19

Family

ID=10580531

Family Applications (1)

Application NumberTitlePriority DateFiling Date
JP61131674AGrantedJPS62283199A (en)1985-06-111986-06-06Oxygen detergent composition

Country Status (11)

CountryLink
US (1)US5133893A (en)
EP (1)EP0205208B1 (en)
JP (1)JPS62283199A (en)
KR (1)KR900004521B1 (en)
AU (1)AU575485B2 (en)
BR (1)BR8602691A (en)
CA (1)CA1288365C (en)
DE (1)DE3686671T2 (en)
GB (1)GB8514708D0 (en)
NO (1)NO166875C (en)
ZA (1)ZA864333B (en)

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Also Published As

Publication numberPublication date
NO166875C (en)1991-09-11
GB8514708D0 (en)1985-07-10
BR8602691A (en)1987-02-03
CA1288365C (en)1991-09-03
AU5847986A (en)1986-12-18
KR870000417A (en)1987-02-18
AU575485B2 (en)1988-07-28
KR900004521B1 (en)1990-06-28
ZA864333B (en)1988-02-24
DE3686671D1 (en)1992-10-15
NO862295L (en)1986-12-12
EP0205208A3 (en)1988-11-09
US5133893A (en)1992-07-28
EP0205208B1 (en)1992-09-09
DE3686671T2 (en)1993-03-04
JPH0134560B2 (en)1989-07-19
EP0205208A2 (en)1986-12-17
NO166875B (en)1991-06-03
NO862295D0 (en)1986-06-09

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